› 2bk2

Electron Microscopy
28Å resolution

The prepore structure of pneumolysin, obtained by fitting the alpha carbon trace of perfringolysin O into a cryo-EM map

Released:
DOI: 10.2210/pdb2bk2/pdb
PDB entry 2bk2 coloured by chain, front view.
PDB entry 2bk2 coloured by chain, side view.
PDB entry 2bk2 coloured by chain, top view.
Source organism: Clostridium perfringens
Primary publication:
Structural basis of pore formation by the bacterial toxin pneumolysin.
Tilley SJ, Orlova EV, Gilbert RJ, Andrew PW, Saibil HR
Cell 121 247-56 (2005)
PMID: 15851031
Related structures: EMD-1106

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo 31-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Perfringolysin O Chain: A
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 50.99 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C2E9 (Residues: 36-500; Coverage: 97%)
Gene names: CPE0163, pfo, pfoA, pfoR
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 28Å
Relevant EMDB volumes: EMD-1106
Expression system: Escherichia coli

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Citations

79 review citations

Mitochondria and cell death: outer membrane permeabilization and beyond.
Tait et al. (2010)
78 more

6 mentions without citation

Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.
Dunstone et al. (2012)
5 more